The ribulose bisphosphate carboxylase/oxygenase of Prochlorothrix hollandica: purification, subunit structure and partial N-terminal sequence analysis of the large subunit.
Ribulose bisphosphate carboxylase/oxygenase was purified to apparent homogeneity from the carboxysomes of Prochlorothrix hollandica. The MW of the native enzyme was estimated to be 560,000 Dalton, comprising large subunits (LSU) of 57,000 Dalton and small subunits (SSU) of 13,000, probably in an 8LSU8SSU quaternary structure. Enzyme activity was maximal at pH 8.0 at 30 degrees C. The requirement of activity for Mg2+ could not be replaced by Mn2+. Co2+, Ca2+ or Cu2+. Amino acid N-terminal sequence analysis of the LSU showed a high degree of conservation when compared to cyanobacterial and chloroplast LSU sequences but was too short to allow a reliable phylogenetic assignment of P. hollandica.
Hawthornthwaite
A M
AM
Department of Biological Sciences, University of Dundee, U.K.
Beanland
T J
TJ
Howe
C J
CJ
Codd
G A
GA
D000595:Amino Acid Sequence; D002499:Centrifugation, Density Gradient; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012273:Ribulose-Bisphosphate Carboxylase / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid
D046911:Macromolecular Substances; D012273:Ribulose-Bisphosphate Carboxylase